RPA-1 from Leishmania amazonensis (LaRPA-1) structurally differs from other eukaryote RPA-1 and interacts with telomeric DNA via its N-terminal OB-fold domain
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Data
2014-12-20
Autores
Pavani, R. S. [UNESP]
Fernandes, C. [UNESP]
Perez, A. M.
Vasconcelos, E. J. R.
Siqueira-Neto, J. L.
Fontes, M. R. [UNESP]
Cano, M. I. N. [UNESP]
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Editor
Elsevier B.V.
Resumo
Replication protein A-1 (RPA-1) is a single-stranded DNA-binding protein involved in DNA metabolism. We previously demonstrated the interaction between LaRPA-1 and telomeric DNA. Here, we expressed and purified truncated mutants of LaRPA-1 and used circular dichroism measurements and molecular dynamics simulations to demonstrate that the tertiary structure of LaRPA-1 differs from human and yeast RPA-1. LaRPA-1 interacts with telomeric ssDNA via its N-terminal OB-fold domain, whereas RPA from higher eukaryotes show different binding modes to ssDNA. Our results show that LaRPA-1 is evolutionary distinct from other RPA-1 proteins and can potentially be used for targeting trypanosomatid telomeres. (C) 2014 Federation of European Biochemical Societies. Published by Elsevier B.V. All rights reserved.
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Palavras-chave
LaRPA-1, Leishmania amazonensis, Telomeres, OB-fold domain, Replication protein A subunit 70 kDa, Replication factor 1
Como citar
Febs Letters. Amsterdam: Elsevier Science Bv, v. 588, n. 24, p. 4740-4748, 2014.